Isozymes of glyceraldehyde‐3‐phosphate dehydrogenase in man and other mammals

Abstract

Multiple electrophoretically distinct forms of glyceraldehyde-3-phosphate dehydrogenase have been observed in human and other mammalian tissues. The human isozymes appear to have essentially the same structural and kinetic properties. An apparent correlation between red-cell age and the relative intensities of the isozymes supports the idea that the isozymes arise as a result of post-translational modification of the polypeptide chain. The possibility that a second locus is involved in the determination of these isozymes is discussed.